Molecular structure of a hyperactive antifreeze protein adsorbed to ice | Zendy

Konrad Meister | Zendy; Carolyn J. Moll | Zendy; Sandipan Chakraborty | Zendy; Biman Jana | Zendy; Arthur L. DeVries | Zendy; Hans Ramløv | Zendy; Huib J. Bakker | Zendy

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Molecular structure of a hyperactive antifreeze protein adsorbed to ice

Author(s) -

Konrad Meister,

Carolyn J. Moll,

Sandipan Chakraborty,

Biman Jana,

Arthur L. DeVries,

Hans Ramløv,

Huib J. Bakker

Publication year - 2019

Publication title -

the journal of chemical physics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.071

H-Index - 357

eISSN - 1089-7690

pISSN - 0021-9606

DOI - 10.1063/1.5090589

Subject(s) - antifreeze protein , ice crystals , adsorption , hydrogen bond , chemistry , molecule , protein adsorption , molecular dynamics , materials science , biochemistry , organic chemistry , computational chemistry , physics , optics

Antifreeze proteins (AFPs) are a unique class of proteins that bind to ice crystal surfaces and arrest their growth. The working mechanism of AFPs is not well understood because, as of yet, it was not possible to perform molecular-scale studies of AFPs adsorbed to the surface of ice. Here, we study the structural properties of an AFP from the insect Rhagium mordax (RmAFP) adsorbed to ice with surface specific heterodyne-detected vibrational sum-frequency generation spectroscopy and molecular dynamic simulations. We find that RmAFP, unlike other proteins, retains its hydrating water molecules upon adsorption to the ice surface. This hydration water has an orientation and hydrogen-bond structure different from the ice surface, thereby inhibiting the insertion of water layers in between the protein and the ice surface.

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